Research workbench
Mineralocorticoid receptor with bound progesterone
Analyse Mineralocorticoid receptor with bound progesterone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AA5
- Type
- protein
- Length
- 510 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mineralocorticoid receptor
- UniProt
- P08235
- Ligands
- STR
- Pockets
- 8 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mineralocorticoid receptor | protein | 255 | 67% helix, 5% strand | P08235 |
| B | Mineralocorticoid receptor | protein | 255 | 69% helix, 5% strand | P08235 |
Ligands and binding sites
- STR · Progesterone · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 178 | 0.83 | 0.97 | 23 | STR |
| 2 | 175 | 0.83 | 0.97 | 23 | STR |
| 3 | 135 | 0.69 | 0.90 | 22 | empty |
| 4 | 143 | 0.66 | 0.87 | 21 | empty |
| 5 | 90 | 0.48 | 0.81 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 558 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P08235
- Elsewhere: RCSB PDB 2AA5 · PDBe 2AA5 · UniProt P08235
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